Specificity in in vitro complementation of -galactosidase from mutant m15 of E. coli.
作者信息
Marinkovic D V, Tang J
出版信息
Biochem Biophys Res Commun. 1971 Dec 3;45(5):1288-93. doi: 10.1016/0006-291x(71)90158-6.
PMID:4944355
Abstract
摘要
相似文献
1
Specificity in in vitro complementation of -galactosidase from mutant m15 of E. coli.大肠杆菌突变体m15的β-半乳糖苷酶体外互补特异性
Biochem Biophys Res Commun. 1971 Dec 3;45(5):1288-93. doi: 10.1016/0006-291x(71)90158-6.
2
A cyanogen bromide fragment of beta-galactosidase from Escherichia coli with alpha-donor activity in complementation of the enzyme from mutant M15.来自大肠杆菌的β-半乳糖苷酶的溴化氰片段，在与突变体M15的酶互补时具有α供体活性。
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Molecular basis of beta-galactosidase alpha-complementation.β-半乳糖苷酶α-互补的分子基础。
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Complementable fraction and complemented enzyme of mutant M15 from Escherichia coli: partial purification by affinity chromatography.大肠杆菌突变体M15的可补体部分和补体酶：通过亲和层析进行部分纯化
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Restoration of beta-galactosidase to Escherichia coli M15. Complementation studies.β-半乳糖苷酶在大肠杆菌M15中的恢复。互补研究。
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引用本文的文献
1
A cyanogen bromide fragment of beta-galactosidase from Escherichia coli with alpha-donor activity in complementation of the enzyme from mutant M15.来自大肠杆菌的β-半乳糖苷酶的溴化氰片段，在与突变体M15的酶互补时具有α供体活性。
Biochem J. 1976 May 1;155(2):209-16. doi: 10.1042/bj1550209.
2
Restoration of beta-galactosidase to Escherichia coli M15. Complementation studies.β-半乳糖苷酶在大肠杆菌M15中的恢复。互补研究。
Biochem J. 1977 Sep 1;165(3):417-23. doi: 10.1042/bj1650417c.
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